The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Protein Dynamism and Evolvability
Abstract
The traditional view that proteins possess absolute functional specificity and a single, fixed structure conflicts with their marked ability to adapt and evolve new functions and structures. We consider an alternative, “avant-garde view” in which proteins are conformationally dynamic and exhibit functional promiscuity. We surmise that these properties are the foundation stones of protein evolvability; they facilitate the divergence of new functions within existing folds and the evolution of entirely new folds. Packing modes of proteins also affect their evolvability, and poorly packed, disordered, and conformationally diverse proteins may exhibit high evolvability. This dynamic view of protein structure, function, and evolvability is extrapolated to describe hypothetical scenarios for the evolution of the early proteins and future research directions in the area of protein dynamism and evolution.
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Citations
Cites
Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871
Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions
Tompa, P., & Fuxreiter, M. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.10.003 · Cited by 1,086
A hierarchy of timescales in protein dynamics is linked to enzyme catalysis
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Recognition Dynamics Up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution
Lange, O. F., Lakomek, N.-A., Farès, C., Schröder, G. F., Walter, K. F. A., Becker, S., Meiler, J., Grubmüller, H., Griesinger, C., & de Groot, B. L. (2008) · Science · doi:10.1126/science.1157092 · Cited by 1,044
Antibody Multispecificity Mediated by Conformational Diversity
James, L. C., Roversi, P., & Tawfik, D. S. (2003) · Science · doi:10.1126/science.1079731 · Cited by 719
Self-citationAllosteric regulation and catalysis emerge via a common route
Goodey, N. M., & Benkovic, S. J. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.98 · Cited by 667
Missense meanderings in sequence space: a biophysical view of protein evolution
DePristo, M. A., Weinreich, D. M., & Hartl, D. L. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1672 · Cited by 650
Enzyme promiscuity: evolutionary and mechanistic aspects
Khersonsky, O., Roodveldt, C., & Tawfik, D. S. (2006) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2006.08.011 · Cited by 641
Self-citationEvolution of Hormone-Receptor Complexity by Molecular Exploitation
Bridgham, J. T., Carroll, S. M., & Thornton, J. W. (2006) · Science · doi:10.1126/science.1123348 · Cited by 599
How Protein Stability and New Functions Trade Off
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Cited by
The role of dynamic conformational ensembles in biomolecular recognition
Boehr, D. D., Nussinov, R., & Wright, P. E. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.232 · Cited by 2,008
Enzyme promiscuity: A mechanistic and evolutionary perspective
Tawfik, O. K. A. D. S. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-030409-143718 · Cited by 1,355
Global dynamics of proteins: bridging between structure and function
Bahar, I., Lezon, T. R., Yang, L.-W., & Eyal, E. (2010) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.093008.131258 · Cited by 610
An introduction to NMR-based approaches for measuring protein dynamics
Kleckner, I. R., & Foster, M. P. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.10.012 · Cited by 561
The role of protein dynamics in the evolution of new enzyme function
Campbell, E., Kaltenbach, M., Correy, G. J., Carr, P. D., Porebski, B. T., Livingstone, E. K., Afriat-Jurnou, L., Buckle, A. M., Weik, M., Hollfelder, F., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2175 · Cited by 311
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Metadata
- Authors
- Tokuriki, N., & Tawfik, D. S.
- Venue
- Science
- Published
- 2009-04-10
- Volume
- 324
- Issue
- 5924
- Pages
- 203-207
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2049888624
- Cited by
- 940
- References
- 45
- FWCI
- 25.81
- Type
- journal article
- Language
- en
- Open access
- closed
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